A preliminary X-ray study of a refolded PTS EIIBfruc protein from Escherichia coli

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Abstract

The phosphoenolpyruvate-carbohydrate phosphotransferase system (PTS) catalyzes the phosphorylation and transportation of its sugar substrates. A sugar-specific enzyme II complex involved in the PTS finally functions to translocate substrates across the membrane. A PTS EIIBfruc protein, a fructose specific EIIB subunit, from Escherichia coli has been cloned, expressed, refolded, purified, and crystallized. The synchrotron data were collected to 2.6 Å from the crystal of a selenomethionine substitute PTS EIIBfruc protein. The crystal belongs to the primitive trigonal space group P3121, with unit-cell parameters of a = 33.4 Å, b = 33.4 Å, c = 154.0 Å, and β = 120.0°. A full structure determination is under way to provide insights into the structure-function relationships of this protein.

Original languageEnglish
Pages (from-to)630-632
Number of pages3
JournalProtein and Peptide Letters
Volume15
Issue number6
DOIs
StatePublished - Jul 2008

Keywords

  • A fructose specific EIIB subunit
  • Crystal
  • Phosphoenolpyruvate-carbohydrate phosphotransferase system
  • Refolding
  • X-ray

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